2j3q

TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH FLUOROPHORE THIOFLAVIN T
(see also AChE inhibitors and substrates (Part III))

 The Torpedo californica acetylcholinesterase (TcAChE) active site consists of two binding subsites. First of them is the "catalytic anionic site" (CAS), which involves catalytic triad Ser200, His440, and Glu327 (colored orange) and the conserved residues Trp84 and Phe330 which also participate in ligands recognition. Another conserved residue Trp279 (colored cyan) is situated at the second binding subsite, termed the "peripheral anionic site" (PAS), ~14 Å from CAS. Thioflavin T is a good example of the PAS-binding AChE inhibitors. Superposition of the crystal structure of the CAS-binding inhibitor edrophonium in complex with TcAChE (2ack) on thioflavin T/TcAChE structure demonstrates that these ligands do not overlapped. Of note, that Phe330, which is part of the CAS, is a single residue interacting with thioflavin T. Only this residue significantly changes its conformation to avoid clashes in comparison to other CAS residues of the edrophonium/TcAChE complex.

About this Structure
2J3Q is a 1 chain structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.

Additional Resources
For additional information, see: Alzheimer's Disease

Reference
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